ID OPGD_ECO27 Reviewed; 551 AA.
AC B7URH4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Glucans biosynthesis protein D {ECO:0000255|HAMAP-Rule:MF_01068};
DE Flags: Precursor;
GN Name=mdoD {ECO:0000255|HAMAP-Rule:MF_01068};
GN Synonyms=opgD {ECO:0000255|HAMAP-Rule:MF_01068};
GN OrderedLocusNames=E2348C_1568;
OS Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=574521;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E2348/69 / EPEC;
RX PubMed=18952797; DOI=10.1128/jb.01238-08;
RA Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT "Complete genome sequence and comparative genome analysis of
RT enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL J. Bacteriol. 191:347-354(2009).
CC -!- FUNCTION: Probably involved in the control of the structural glucose
CC backbone of osmoregulated periplasmic glucans (OPGs).
CC {ECO:0000255|HAMAP-Rule:MF_01068}.
CC -!- PATHWAY: Glycan metabolism; osmoregulated periplasmic glucan (OPG)
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01068}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_01068}.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has not been experimentally proven.
CC -!- SIMILARITY: Belongs to the OpgD/OpgG family. {ECO:0000255|HAMAP-
CC Rule:MF_01068}.
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DR EMBL; FM180568; CAS09116.1; -; Genomic_DNA.
DR RefSeq; WP_000375975.1; NC_011601.1.
DR AlphaFoldDB; B7URH4; -.
DR SMR; B7URH4; -.
DR KEGG; ecg:E2348C_1568; -.
DR HOGENOM; CLU_023403_2_0_6; -.
DR UniPathway; UPA00637; -.
DR Proteomes; UP000008205; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0009250; P:glucan biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 2.70.98.10; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR HAMAP; MF_01068; MdoD_OpgD; 1.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR023724; Glucan_biosyn_MdoD.
DR InterPro; IPR014438; Glucan_biosyn_MdoG/MdoD.
DR InterPro; IPR007444; Glucan_biosyn_MdoG_C.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR NCBIfam; TIGR01409; TAT_signal_seq; 1.
DR PANTHER; PTHR30504; GLUCANS BIOSYNTHESIS PROTEIN; 1.
DR PANTHER; PTHR30504:SF3; GLUCANS BIOSYNTHESIS PROTEIN D; 1.
DR Pfam; PF04349; MdoG; 1.
DR PIRSF; PIRSF006281; MdoG; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Periplasm; Reference proteome; Signal.
FT SIGNAL 1..32
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01068"
FT CHAIN 33..551
FT /note="Glucans biosynthesis protein D"
FT /id="PRO_1000149745"
SQ SEQUENCE 551 AA; 62761 MW; E78B169004C4E893 CRC64;
MDRRRFIKGS MAMAAVCGTS GIASLFSQAA FAADSDIADG QTQRFDLSIL QSMAHDLAQT
AWRGAPRPLP DTLATMTPQA YNSIQYDAEK SLWHNVENRQ LDAQFFHMGM GFRRRVRMFS
VDPATHLARE IHFRPELFKY NDAGVDTKQL EGQSDLGFAG FRVFKAPELA RRDVVSFLGA
SYFRAVDDTY QYGLSARGLA IDTYTDSKEE FPDFTAFWFD TVKPGATTFT VYALLDSASI
TGAYKFTIHC EKNQVIMDVE NHLYARKDIK QLGIAPMTSM FSCGTNERRM CDTIHPQIHD
SDRLSMWRGN GEWICRPLNN PQKLQFNAYT DNNPKGFGLL QLDRDFSHYQ DIMGWYNKRP
SLWVEPRNKW GKGTIGLMEI PTTGETLDNI VCFWQPEKAV KAGDEFAFQY RLYWSAQPPV
HCPLARVMAT RTGMGGFPEG WAPGEHYPEK WARRFAVDFV GGDLKAAAPK GIEPVITLSS
GEAKQIEILY IEPIDGYRIQ FDWYPTSDST DPVDMRMYLR CQGDAISETW LYQYFPPAPD
KRQYVDDRVM S
//
